ID A0A3Q0R342_AMPCI Unreviewed; 273 AA.
AC A0A3Q0R342;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Heme oxygenase {ECO:0000256|PIRNR:PIRNR000343};
DE EC=1.14.14.18 {ECO:0000256|PIRNR:PIRNR000343};
GN Name=HMOX1 {ECO:0000313|Ensembl:ENSACIP00000004597.1};
OS Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC Cichlasomatinae; Heroini; Amphilophus.
OX NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000004597.1, ECO:0000313|Proteomes:UP000261340};
RN [1] {ECO:0000313|Ensembl:ENSACIP00000004597.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=heme b + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] =
CC biliverdin IXalpha + CO + Fe(2+) + H(+) + 3 H2O + 3 oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:21764, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17245,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:57618, ChEBI:CHEBI:57991,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:60344; EC=1.14.14.18;
CC Evidence={ECO:0000256|PIRNR:PIRNR000343};
CC -!- SIMILARITY: Belongs to the heme oxygenase family.
CC {ECO:0000256|PIRNR:PIRNR000343}.
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DR AlphaFoldDB; A0A3Q0R342; -.
DR Ensembl; ENSACIT00000004743.1; ENSACIP00000004597.1; ENSACIG00000003536.1.
DR GeneTree; ENSGT00390000017673; -.
DR OMA; FAYLHVM; -.
DR Proteomes; UP000261340; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004392; F:heme oxygenase (decyclizing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006788; P:heme oxidation; IEA:UniProtKB-UniRule.
DR CDD; cd19165; HemeO; 1.
DR Gene3D; 1.20.910.10; Heme oxygenase-like; 1.
DR InterPro; IPR002051; Haem_Oase.
DR InterPro; IPR016053; Haem_Oase-like.
DR InterPro; IPR016084; Haem_Oase-like_multi-hlx.
DR PANTHER; PTHR10720; HEME OXYGENASE; 1.
DR PANTHER; PTHR10720:SF1; HEME OXYGENASE 1; 1.
DR Pfam; PF01126; Heme_oxygenase; 1.
DR PIRSF; PIRSF000343; Haem_Oase; 1.
DR PRINTS; PR00088; HAEMOXYGNASE.
DR SUPFAM; SSF48613; Heme oxygenase-like; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Heme {ECO:0000256|PIRNR:PIRNR000343, ECO:0000256|PIRSR:PIRSR000343-1};
KW Iron {ECO:0000256|PIRNR:PIRNR000343, ECO:0000256|PIRSR:PIRSR000343-2};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR000343,
KW ECO:0000256|PIRSR:PIRSR000343-2}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 16
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000256|PIRSR:PIRSR000343-1"
FT BINDING 23
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000343-2"
FT BINDING 132
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000256|PIRSR:PIRSR000343-1"
FT BINDING 180
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000256|PIRSR:PIRSR000343-1"
SQ SEQUENCE 273 AA; 31046 MW; 13EF8FD7451DE282 CRC64;
FHVQNQQHPD LSEQIKKVTK ESHVRAENTE LMLSFQRGKV TLPQYKLLLC SLYEIYQALE
EALDRNSNHP NVAPIYFPAE LARLRSIEKD LEYFYGQDWR EKIVVPAATK RYCHRLRQIG
KENPEFLLAH AYTRYLGDLS GGQVLGRIAQ KSMGLKNGDG LSFFAFPGVS SPNLFKQLYR
SRMNSVELTE EERNGVLEEA VRAFEFNIQV FEDLQKMLNV SDNKLQSSLT QSKPVKANTL
HVPGTSVYTS SLLRMVLGLF VALATVSVGI YAL
//
